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Volumn 71, Issue 5, 2003, Pages 2384-2393

Aae, an autotransporter involved in adhesion of Actinobacillus actinomycetemcomitans to epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; CARRIER PROTEIN; IMMUNOGLOBULIN A1; LACTOFERRIN; PROTEIN AAE; PROTEINASE; SPECTINOMYCIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 0037407497     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.5.2384-2393.2003     Document Type: Article
Times cited : (55)

References (60)
  • 2
    • 0028905303 scopus 로고
    • Inhibitory effect of lactoferrin on the adhesion of Actinobacillus actinomycetemcomitans and Prevotella intermedia to fibroblasts and epithelial cells
    • Alugupalli, K. R., and S. Kalfas. 1995. Inhibitory effect of lactoferrin on the adhesion of Actinobacillus actinomycetemcomitans and Prevotella intermedia to fibroblasts and epithelial cells. APMIS 103:154-160.
    • (1995) APMIS , vol.103 , pp. 154-160
    • Alugupalli, K.R.1    Kalfas, S.2
  • 3
    • 0030763459 scopus 로고    scopus 로고
    • Characterization of the lactoferrin-dependent inhibition of the adhesion of Actinobacillus actinomycetemcomitans, Prevotella intermedia and Prevotella nigrescens to fibroblasts and to a reconstituted basement membrane
    • Alugupalli, K. R., and S. Kalfas. 1997. Characterization of the lactoferrin-dependent inhibition of the adhesion of Actinobacillus actinomycetemcomitans, Prevotella intermedia and Prevotella nigrescens to fibroblasts and to a reconstituted basement membrane. APMIS 105:680-688.
    • (1997) APMIS , vol.105 , pp. 680-688
    • Alugupalli, K.R.1    Kalfas, S.2
  • 5
    • 0027184837 scopus 로고
    • The anomalous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues
    • Armstrong, D. J., and A. Roman. 1993. The anomalous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues. Biochem. Biophys. Res. Commun. 192:1380-1387.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 1380-1387
    • Armstrong, D.J.1    Roman, A.2
  • 6
    • 0018868141 scopus 로고
    • Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms
    • Arnold, R. R., M. Brewer, and J. J. Gauthier. 1980. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect. Immun. 28:893-898.
    • (1980) Infect. Immun. , vol.28 , pp. 893-898
    • Arnold, R.R.1    Brewer, M.2    Gauthier, J.J.3
  • 9
    • 0034816350 scopus 로고    scopus 로고
    • Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase
    • Bhattacharjee, M. K., S. C. Kachlany, D. H. Fine, and D. H. Figurski. 2001. Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase. J. Bacteriol. 183:5927-5936.
    • (2001) J. Bacteriol. , vol.183 , pp. 5927-5936
    • Bhattacharjee, M.K.1    Kachlany, S.C.2    Fine, D.H.3    Figurski, D.H.4
  • 10
    • 0035061098 scopus 로고    scopus 로고
    • Porphyromonas gingivalis gingipains and adhesion to epithelial cells
    • Chen, T., K. Nakayama, L. Belliveau, and M. J. Duncan. 2001. Porphyromonas gingivalis gingipains and adhesion to epithelial cells. Infect. Immun. 69:3048-3056.
    • (2001) Infect. Immun. , vol.69 , pp. 3048-3056
    • Chen, T.1    Nakayama, K.2    Belliveau, L.3    Duncan, M.J.4
  • 11
    • 0023392355 scopus 로고
    • Tissue localization of Actinobacillus actinomycetemcomitans in human periodontitis. I. Light, immunofluorescence and electron microscopic studies
    • Christersson, L. A., B. Albini, J. J. Zambon, U. M. Wikesjo, and R. J. Genco. 1987. Tissue localization of Actinobacillus actinomycetemcomitans in human periodontitis. I. Light, immunofluorescence and electron microscopic studies. J. Periodontol. 58:529-539.
    • (1987) J. Periodontol. , vol.58 , pp. 529-539
    • Christersson, L.A.1    Albini, B.2    Zambon, J.J.3    Wikesjo, U.M.4    Genco, R.J.5
  • 12
    • 0033555520 scopus 로고    scopus 로고
    • The gene, ial4, associated with invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5′-polyphosphate
    • Conyers, G. B., and M. J. Bessman. 1999. The gene, ial4, associated with invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5′-polyphosphate. J. Biol. Chem. 274:1203-1206.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1203-1206
    • Conyers, G.B.1    Bessman, M.J.2
  • 13
    • 0034947069 scopus 로고    scopus 로고
    • Evolution of an autotransporter: Domain shuffling and lateral transfer from pathogenic Haemophilus to Neisseria
    • Davis, J., A. L. Smith, W. R. Hughes, and M. Golomb. 2001. Evolution of an autotransporter: domain shuffling and lateral transfer from pathogenic Haemophilus to Neisseria. J. Bacteriol. 183:4626-4635.
    • (2001) J. Bacteriol. , vol.183 , pp. 4626-4635
    • Davis, J.1    Smith, A.L.2    Hughes, W.R.3    Golomb, M.4
  • 14
    • 0031770094 scopus 로고    scopus 로고
    • Improved antibiotic-resistance cassettes through restriction site elimination using Pfu DNA polymerase PCR
    • Dennis, J. J., and G. J. Zylstra. 1998. Improved antibiotic-resistance cassettes through restriction site elimination using Pfu DNA polymerase PCR. BioTechniques 25:772-776.
    • (1998) BioTechniques , vol.25 , pp. 772-776
    • Dennis, J.J.1    Zylstra, G.J.2
  • 15
    • 0014690895 scopus 로고
    • Observations on molecular weight determinations on polyacrylamide gel
    • Dunker, A. K., and R. R. Rueckert. 1969. Observations on molecular weight determinations on polyacrylamide gel. J. Biol. Chem. 244:5074-5080.
    • (1969) J. Biol. Chem. , vol.244 , pp. 5074-5080
    • Dunker, A.K.1    Rueckert, R.R.2
  • 16
    • 0019943680 scopus 로고
    • Whole-bacterial cell enzyme-linked immunosorbent assay for Streptococcus sanguis fimbrial antigens
    • Elder, B. L., D. K. Boraker, and P. M. Fives-Taylor. 1982. Whole-bacterial cell enzyme-linked immunosorbent assay for Streptococcus sanguis fimbrial antigens. J. Clin. Microbiol. 16:141-144.
    • (1982) J. Clin. Microbiol. , vol.16 , pp. 141-144
    • Elder, B.L.1    Boraker, D.K.2    Fives-Taylor, P.M.3
  • 17
    • 0023815539 scopus 로고
    • Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin
    • Ellison, R. T., III, T. J. Giehl, and F. M. LaForce. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
    • (1988) Infect. Immun. , vol.56 , pp. 2774-2781
    • Ellison R.T. III1    Giehl, T.J.2    LaForce, F.M.3
  • 18
    • 0028625324 scopus 로고
    • The effects of lactoferrin on gram-negative bacteria
    • T. W. Hutchins, S. V. Rumball, and B. Lonnerdal (ed.). Plenum Press, New York, N.Y.
    • Ellison, R. T., III. 1994. The effects of lactoferrin on gram-negative bacteria, p. 71-90. In T. W. Hutchins, S. V. Rumball, and B. Lonnerdal (ed.), Lactoferrin: structure and function. Plenum Press, New York, N.Y.
    • (1994) Lactoferrin: Structure and Function , pp. 71-90
    • Ellison R.T. III1
  • 19
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay, B. B., and S. Falkow. 1997. Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 61:136-169.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 20
    • 0033614807 scopus 로고    scopus 로고
    • The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme
    • Fukasawa, K., K. M. Fukasawa, H. Iwamoto, J. Hirose, and H. Harada. 1999. The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme. Biochemistry 38:8299-8303.
    • (1999) Biochemistry , vol.38 , pp. 8299-8303
    • Fukasawa, K.1    Fukasawa, K.M.2    Iwamoto, H.3    Hirose, J.4    Harada, H.5
  • 21
    • 0036490951 scopus 로고    scopus 로고
    • The Rickettsia prowazekii invasion gene homolog (invA) encodes a nudix hydrolase active on adenosine (5′)-pentaphospho-(5′)-adenosine
    • Gaywee, J., W. Xu, S. Radulovic, M. J. Bessman, and A. F. Azad. 2002. The Rickettsia prowazekii invasion gene homolog (invA) encodes a nudix hydrolase active on adenosine (5′)-pentaphospho-(5′)-adenosine. Mol. Cell Proteomics 1:179-183.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 179-183
    • Gaywee, J.1    Xu, W.2    Radulovic, S.3    Bessman, M.J.4    Azad, A.F.5
  • 23
    • 0035014876 scopus 로고    scopus 로고
    • The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide
    • Haug, B. E., and J. S. Svendsen. 2001. The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide. J. Pept. Sci. 7:190-196.
    • (2001) J. Pept. Sci. , vol.7 , pp. 190-196
    • Haug, B.E.1    Svendsen, J.S.2
  • 24
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson, I. R., and J. P. Nataro. 2001. Virulence functions of autotransporter proteins. Infect. Immun. 69:1231-1243.
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 25
    • 0032246189 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein
    • Hendrixson, D. R., and J. W. St Geme III. 1998. The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein. Mol. Cell 2:841-850.
    • (1998) Mol. Cell. , vol.2 , pp. 841-850
    • Hendrixson, D.R.1    St Geme J.W. III2
  • 26
    • 0025424746 scopus 로고
    • Colonial variation and fimbriation of Actinobacillus actinomycetemcomitans
    • Inouye, T., H. Ohta, S. Kokeguchi, K. Fukui, and K. Kato. 1990. Colonial variation and fimbriation of Actinobacillus actinomycetemcomitans. FEMS Microbiol. Lett. 57:13-17.
    • (1990) FEMS Microbiol. Lett. , vol.57 , pp. 13-17
    • Inouye, T.1    Ohta, H.2    Kokeguchi, S.3    Fukui, K.4    Kato, K.5
  • 27
    • 0033758854 scopus 로고    scopus 로고
    • Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea
    • Kachlany, S. C., P. J. Planet, M. K. Bhattacharjee, E. Kollia, R. DeSalle, D. H. Fine, and D. H. Figurski. 2000. Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea. J. Bacteriol. 182:6169-6176.
    • (2000) J. Bacteriol. , vol.182 , pp. 6169-6176
    • Kachlany, S.C.1    Planet, P.J.2    Bhattacharjee, M.K.3    Kollia, E.4    DeSalle, R.5    Fine, D.H.6    Figurski, D.H.7
  • 28
    • 0023736956 scopus 로고
    • Killing of Actinobacillus actinomycetemcomitans by human lactoferrin
    • Kalmar, J. R., and R. R. Arnold. 1988. Killing of Actinobacillus actinomycetemcomitans by human lactoferrin. Infect. Immun. 56:2552-2557.
    • (1988) Infect. Immun. , vol.56 , pp. 2552-2557
    • Kalmar, J.R.1    Arnold, R.R.2
  • 29
    • 0242657569 scopus 로고    scopus 로고
    • DNA fragments of Actinobacillus actinomycetemcomitans involved in invasion of KB cells
    • Laing Gibbard, L. P., G. Lepine, and R. P. Ellen. 1998. DNA fragments of Actinobacillus actinomycetemcomitans involved in invasion of KB cells. J. Dent. Res. 77(SI-B):770.
    • (1998) J. Dent. Res. , vol.77 , Issue.SI-B , pp. 770
    • Laing Gibbard, L.P.1    Lepine, G.2    Ellen, R.P.3
  • 30
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay, P. F., and M. Viljoen. 1995. Lactoferrin: a general review. Haematologica 80:252-267.
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 31
    • 0001343349 scopus 로고
    • Family III. Pasteurellaceae
    • N. R. Kreig (ed.), The Williams & Wilkins Co., Baltimore, Md
    • Mannheim, W. 1984. Family III. Pasteurellaceae, p. 550-575. In N. R. Kreig (ed.), Bergey's manual of systematic bacteriology, The Williams & Wilkins Co., Baltimore, Md.
    • (1984) Bergey's Manual of Systematic Bacteriology , pp. 550-575
    • Mannheim, W.1
  • 32
    • 0031426870 scopus 로고
    • Models of invasion of enteric and periodontal pathogens into epithelial cells: A comparative analysis
    • Meyer, D. H., and P. M. Fives-Taylor. 1993. Models of invasion of enteric and periodontal pathogens into epithelial cells: a comparative analysis. Crit. Rev. Oral Biol. Med. 8:389-409.
    • (1993) Crit. Rev. Oral Biol. Med. , vol.8 , pp. 389-409
    • Meyer, D.H.1    Fives-Taylor, P.M.2
  • 33
    • 0027451950 scopus 로고
    • Evidence that extracellular components function in adherence of Actinobacillus actinomycetemcomitans to epithelial cells
    • Meyer, D. H., and P. M. Fives-Taylor. 1993. Evidence that extracellular components function in adherence of Actinobacillus actinomycetemcomitans to epithelial cells. Infect. Immun. 61:4933-4936.
    • (1993) Infect. Immun. , vol.61 , pp. 4933-4936
    • Meyer, D.H.1    Fives-Taylor, P.M.2
  • 34
    • 0028118505 scopus 로고
    • Characteristics of adherence of Actinobacillus actinomycetemcomitans to epithelial cells
    • Meyer, D. H., and P. M. Fives-Taylor. 1994. Characteristics of adherence of Actinobacillus actinomycetemcomitans to epithelial cells. Infect. Immun. 62: 928-935.
    • (1994) Infect. Immun. , vol.62 , pp. 928-935
    • Meyer, D.H.1    Fives-Taylor, P.M.2
  • 35
    • 0030054509 scopus 로고    scopus 로고
    • Invasion of epithelial cells by Actinobacillus actinomycetemcomitans: A dynamic, multistep process
    • Meyer, D. H., J. E. Lippmann, and P. M. Fives-Taylor. 1996. Invasion of epithelial cells by Actinobacillus actinomycetemcomitans: a dynamic, multistep process. Infect. Immun. 64:2988-2997.
    • (1996) Infect. Immun. , vol.64 , pp. 2988-2997
    • Meyer, D.H.1    Lippmann, J.E.2    Fives-Taylor, P.M.3
  • 36
    • 0025915022 scopus 로고
    • Evidence for invasion of a human oral cell line by Actinobacillus actinomycetemcomitans
    • Meyer, D. H., P. K. Sreenivasan, and P. M. Fives-Taylor. 1991. Evidence for invasion of a human oral cell line by Actinobacillus actinomycetemcomitans. Infect. Immun. 59:2719-2726.
    • (1991) Infect. Immun. , vol.59 , pp. 2719-2726
    • Meyer, D.H.1    Sreenivasan, P.K.2    Fives-Taylor, P.M.3
  • 37
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170:2575-2583.
    • (1988) J. Bacteriol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 38
    • 0028101001 scopus 로고
    • Adhesion of Actinobacillus actinomycetemcomitans to a human oral cell line
    • Mintz, K. P., and P. M. Fives-Taylor. 1994. Adhesion of Actinobacillus actinomycetemcomitans to a human oral cell line. Infect. Immun. 62:3672-2678.
    • (1994) Infect. Immun. , vol.62 , pp. 3672-2678
    • Mintz, K.P.1    Fives-Taylor, P.M.2
  • 39
    • 0034441341 scopus 로고    scopus 로고
    • impA, a gene coding for an inner membrane protein, influences colonial morphology of Actinobacillus actinomycetemcomitans
    • Mintz, K. P., and P. M. Fives-Taylor. 2000. impA, a gene coding for an inner membrane protein, influences colonial morphology of Actinobacillus actinomycetemcomitans. Infect. Immun. 68:6580-6586.
    • (2000) Infect. Immun. , vol.68 , pp. 6580-6586
    • Mintz, K.P.1    Fives-Taylor, P.M.2
  • 40
    • 0028953917 scopus 로고
    • Characterization of a two-gene locus from Bartonella bacilliformis associated with the ability to invade human erythrocytes
    • Mitchell, S. J., and M. F. Minnick. 1995. Characterization of a two-gene locus from Bartonella bacilliformis associated with the ability to invade human erythrocytes. Infect. Immun. 63:1552-1562.
    • (1995) Infect. Immun. , vol.63 , pp. 1552-1562
    • Mitchell, S.J.1    Minnick, M.F.2
  • 41
    • 0025933503 scopus 로고
    • Expert system for predicting protein localization sites in gram-negative bacteria
    • Nakai, K., and M. Kanehisa. 1991. Expert system for predicting protein localization sites in gram-negative bacteria. Proteins 11:95-110.
    • (1991) Proteins , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 42
    • 0031809272 scopus 로고    scopus 로고
    • Characterization of serologically nontypeable Actinobacillus actinomycetemcomitans isolates
    • Paju, S., M. Saarela, S. Alaluusua, P. Fives-Taylor, and S. Asikainen. 1998. Characterization of serologically nontypeable Actinobacillus actinomycetemcomitans isolates. J. Clin. Microbiol. 36:2019-2022.
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 2019-2022
    • Paju, S.1    Saarela, M.2    Alaluusua, S.3    Fives-Taylor, P.4    Asikainen, S.5
  • 43
    • 0029913412 scopus 로고    scopus 로고
    • Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis
    • Pike, R. N., J. Potempa, W. McGraw, T. H. Coetzer, and J. Travis. 1996. Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis. J. Bacteriol. 178:2876-2882.
    • (1996) J. Bacteriol. , vol.178 , pp. 2876-2882
    • Pike, R.N.1    Potempa, J.2    McGraw, W.3    Coetzer, T.H.4    Travis, J.5
  • 44
    • 0035957004 scopus 로고    scopus 로고
    • Phylogeny of genes for secretion NTPases: Identification of the widespread tadA subfamily and development of a diagnostic key for gene classification
    • Planet, P. J., S. C. Kachlany, R. DeSalle, and D. H. Figurski. 2001. Phylogeny of genes for secretion NTPases: identification of the widespread tadA subfamily and development of a diagnostic key for gene classification. Proc. Natl. Acad. Sci. USA 98:2503-2508.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2503-2508
    • Planet, P.J.1    Kachlany, S.C.2    DeSalle, R.3    Figurski, D.H.4
  • 45
    • 0032514621 scopus 로고    scopus 로고
    • Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae
    • Qiu, J., D. R. Hendrixson, E. N. Baker, T. F. Murphy, J. W. St Geme III, and A. G. Plaut. 1998. Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc. Natl. Acad. Sci. USA 95:12641-12646.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12641-12646
    • Qiu, J.1    Hendrixson, D.R.2    Baker, E.N.3    Murphy, T.F.4    St Geme J.W. III5    Plaut, A.G.6
  • 47
    • 0035081315 scopus 로고    scopus 로고
    • Intracellular Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in buccal epithelial cells collected from human subjects
    • Rudney, J. D., R. Chen, and G. J. Sedgewick. 2001. Intracellular Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in buccal epithelial cells collected from human subjects. Infect. Immun. 69:2700-2707.
    • (2001) Infect. Immun. , vol.69 , pp. 2700-2707
    • Rudney, J.D.1    Chen, R.2    Sedgewick, G.J.3
  • 48
    • 0242405747 scopus 로고    scopus 로고
    • The Actinobacillus actinomycetemcomitans apaH gene is implicated in invasion of epithelial cells
    • Saarela, M., J. E. Lippmann, D. H. Meyer, and P. M. Fives-Taylor. 1999. The Actinobacillus actinomycetemcomitans apaH gene is implicated in invasion of epithelial cells. J. Dent. Res. 78(Spec. issue):1225.
    • (1999) J. Dent. Res. , vol.78 , Issue.SPEC. ISSUE , pp. 1225
    • Saarela, M.1    Lippmann, J.E.2    Meyer, D.H.3    Fives-Taylor, P.M.4
  • 50
    • 0034827946 scopus 로고    scopus 로고
    • Antifungal effects of lysozyme and lactoferrin against genetically similar, sequential Candida albicans isolates from a human immunodeficiency virus-infected southern Chinese cohort
    • Samaranayake, Y. H., L. P. Samaranayake, E. H. Pow, V. T. Beena, and K. W. Yeung. 2001. Antifungal effects of lysozyme and lactoferrin against genetically similar, sequential Candida albicans isolates from a human immunodeficiency virus-infected southern Chinese cohort. J. Clin. Microbiol. 39:3296-3302.
    • (2001) J. Clin. Microbiol. , vol.39 , pp. 3296-3302
    • Samaranayake, Y.H.1    Samaranayake, L.P.2    Pow, E.H.3    Beena, V.T.4    Yeung, K.W.5
  • 51
    • 0028220766 scopus 로고
    • Isolation and characterization of deletion derivatives of pDL282, an Actinobacillus actinomycetemcomitans/Escherichia coli shuttle plasmid
    • Sreenivasan, P. K., and P. M. Fives-Taylor. 1994. Isolation and characterization of deletion derivatives of pDL282, an Actinobacillus actinomycetemcomitans/Escherichia coli shuttle plasmid. Plasmid 31:207-214.
    • (1994) Plasmid , vol.31 , pp. 207-214
    • Sreenivasan, P.K.1    Fives-Taylor, P.M.2
  • 52
    • 0027469567 scopus 로고
    • Requirements for invasion of epithelial cells by Actinobacillus actinomycetemcomitans
    • Sreenivasan, P. K., D. H. Meyer, and P. M. Fives-Taylor. 1993. Requirements for invasion of epithelial cells by Actinobacillus actinomycetemcomitans. Infect. Immun. 61:1239-1245.
    • (1993) Infect. Immun. , vol.61 , pp. 1239-1245
    • Sreenivasan, P.K.1    Meyer, D.H.2    Fives-Taylor, P.M.3
  • 53
    • 0025746336 scopus 로고
    • Transformation of Actinobacillus actinomycetemcomitans by electroporation, utilizing constructed shuttle plasmids
    • Sreenivasan, P. K., D. J. LeBlanc, L. N. Lee, and P. M. Fives-Taylor. 1991. Transformation of Actinobacillus actinomycetemcomitans by electroporation, utilizing constructed shuttle plasmids. Infect. Immun. 59:4621-4627.
    • (1991) Infect. Immun. , vol.59 , pp. 4621-4627
    • Sreenivasan, P.K.1    LeBlanc, D.J.2    Lee, L.N.3    Fives-Taylor, P.M.4
  • 54
    • 0033765760 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated
    • St Geme, J. W., III, and D. Cutter. 2000. The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated. J. Bacteriol. 182:6005-6013.
    • (2000) J. Bacteriol. , vol.182 , pp. 6005-6013
    • St. Geme J.W. III1    Cutter, D.2
  • 55
    • 0027987985 scopus 로고
    • A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells
    • St Geme, J. W., III, M. L. de la Morena, and S. Falkow. 1994. A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells. Mol. Microbiol. 14:217-233.
    • (1994) Mol. Microbiol. , vol.14 , pp. 217-233
    • St. Geme J.W. III1    De la Morena, M.L.2    Falkow, S.3
  • 56
    • 0028100792 scopus 로고
    • Isolation and identification of eukaryotic receptors promoting bacterial internalization
    • Van Nhieu, G. T., and R. R. Isberg. 1994. Isolation and identification of eukaryotic receptors promoting bacterial internalization. Methods Enzymol. 236:307-318.
    • (1994) Methods Enzymol. , vol.236 , pp. 307-318
    • Van Nhieu, G.T.1    Isberg, R.R.2
  • 57
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 58
    • 0022991840 scopus 로고
    • Dephosphorylation of sea urchin sperm guanylate cyclase during fertilization
    • Ward, G. E., G. W. Moy, and V. D. Vacquier. 1986. Dephosphorylation of sea urchin sperm guanylate cyclase during fertilization. Adv. Exp. Med. Biol. 207:359-382.
    • (1986) Adv. Exp. Med. Biol. , vol.207 , pp. 359-382
    • Ward, G.E.1    Moy, G.W.2    Vacquier, V.D.3
  • 59
    • 0027465990 scopus 로고    scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison III. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
    • Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison R.T. III4
  • 60
    • 0021911144 scopus 로고    scopus 로고
    • Actinobacillus actinomycetemcomitans in human periodontal disease
    • 19865
    • Zambon, J. J. 19865. Actinobacillus actinomycetemcomitans in human periodontal disease. J. Clin. Periodontol. 12:1-20.
    • J. Clin. Periodontol. , vol.12 , pp. 1-20
    • Zambon, J.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.